Phospholipid-hydroperoxide glutathione peroxidase
In enzymology, a phospholipid-hydroperoxide glutathione peroxidase (EC 1.11.1.12) is an enzyme that catalyzes the chemical reaction
- 2 glutathione + a lipid hydroperoxide glutathione disulfide + lipid + 2 H2O
phospholipid-hydroperoxide glutathione peroxidase | |||||||||
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Identifiers | |||||||||
EC no. | 1.11.1.12 | ||||||||
CAS no. | 97089-70-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Thus, the two substrates of this enzyme are glutathione and lipid hydroperoxide, whereas its 3 products are glutathione disulfide, lipid, and H2O.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is glutathione:lipid-hydroperoxide oxidoreductase. Other names in common use include peroxidation-inhibiting protein, PHGPX, peroxidation-inhibiting protein: peroxidase, glutathione, (phospholipid hydroperoxide-reducing), phospholipid hydroperoxide glutathione peroxidase, hydroperoxide glutathione peroxidase, or glutathione peroxidase 4 (GPX4). This enzyme participates in glutathione metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2GS3 and 2OBI.
References
- Ursini F, Maiorino M, Gregolin C (1985). "The selenoenzyme phospholipid hydroperoxide glutathione peroxidase". Biochim. Biophys. Acta. 839 (1): 62–70. doi:10.1016/0304-4165(85)90182-5. PMID 3978121.